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Journal Article

Spatial-proteomics reveals phospho-signaling dynamics at subcellular resolution


Steigerwald,  Sophia
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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Martinez-Val, A., Bekker-Jensen, D. B., Steigerwald, S., Koenig, C., Ostergaard, O., Mehta, A., et al. (2021). Spatial-proteomics reveals phospho-signaling dynamics at subcellular resolution. Nature Communications, 12(1): 7113. doi:10.1038/s41467-021-27398-y.

Cite as: https://hdl.handle.net/21.11116/0000-0009-C611-4
Dynamic change in subcellular localization of signaling proteins is a general concept that eukaryotic cells evolved for eliciting a coordinated response to stimuli. Mass spectrometry-based proteomics in combination with subcellular fractionation can provide comprehensive maps of spatio-temporal regulation of protein networks in cells, but involves laborious workflows that does not cover the phospho-proteome level. Here we present a high-throughput workflow based on sequential cell fractionation to profile the global proteome and phospho-proteome dynamics across six distinct subcellular fractions. We benchmark the workflow by studying spatio-temporal EGFR phospho-signaling dynamics in vitro in HeLa cells and in vivo in mouse tissues. Finally, we investigate the spatio-temporal stress signaling, revealing cellular relocation of ribosomal proteins in response to hypertonicity and muscle contraction. Proteomics data generated in this study can be explored through https://SpatialProteoDynamics.github.io.